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Conserved domains on  [gi|488370374|ref|WP_002439759|]
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MULTISPECIES: ribonuclease HI family protein [Staphylococcus]

Protein Classification

ribonuclease HI family protein( domain architecture ID 10174584)

ribonuclease HI family protein such as type 1 ribonuclease H, which is involved in the removal of RNA from RNA/DNA hybrids during DNA replication, repair and transcription; similar to Enterococcus faecalis hydrolase EbsB

CATH:  3.30.420.10
EC:  3.-.-.-
Gene Ontology:  GO:0004523|GO:0003676|GO:0000287|GO:0043137
PubMed:  19228198|19228197|16093691|16232566|2177653
SCOP:  4000541

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNase_HI_like cd09279
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ...
 3-125 1.19e-41

RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Most archaeal genomes contain only type 2 RNase H (RNase HII); however, a few contain RNase HI as well. Although archaeal RNase HI sequences conserve the DEDD active-site motif, they lack other common features important for catalytic function, such as the basic protrusion region. Archaeal RNase HI homologs are more closely related to retroviral RNase HI than bacterial and eukaryotic type I RNase H in enzymatic properties.


:

Pssm-ID: 260011 [Multi-domain]  Cd Length: 128  Bit Score: 134.14  E-value: 1.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374   3 KIHFDAATKGNPGRSACAIIIK-ENSQRYTFTHDLGE-MDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSMM-Q 79
Cdd:cd09279    2 TLYFDGASRGNPGPAGAGVVIYsPGGEVLELSERLGFpATNNEAEYEALIAGLELALELGAEKLEIYGDSQLVVNQLNgE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488370374  80 GKVKNAKFKVYFENIEILEQSFDLMFVRWIPRKQNKEANQLAQQTL 125
Cdd:cd09279   82 YKVKNERLKPLLEKVLELLAKFELVELKWIPREQNKEADALANQAL 127
 
Name Accession Description Interval E-value
RNase_HI_like cd09279
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ...
 3-125 1.19e-41

RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Most archaeal genomes contain only type 2 RNase H (RNase HII); however, a few contain RNase HI as well. Although archaeal RNase HI sequences conserve the DEDD active-site motif, they lack other common features important for catalytic function, such as the basic protrusion region. Archaeal RNase HI homologs are more closely related to retroviral RNase HI than bacterial and eukaryotic type I RNase H in enzymatic properties.


Pssm-ID: 260011 [Multi-domain]  Cd Length: 128  Bit Score: 134.14  E-value: 1.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374   3 KIHFDAATKGNPGRSACAIIIK-ENSQRYTFTHDLGE-MDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSMM-Q 79
Cdd:cd09279    2 TLYFDGASRGNPGPAGAGVVIYsPGGEVLELSERLGFpATNNEAEYEALIAGLELALELGAEKLEIYGDSQLVVNQLNgE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488370374  80 GKVKNAKFKVYFENIEILEQSFDLMFVRWIPRKQNKEANQLAQQTL 125
Cdd:cd09279   82 YKVKNERLKPLLEKVLELLAKFELVELKWIPREQNKEADALANQAL 127
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
1-125 5.43e-29

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 102.23  E-value: 5.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374   1 MAKIHFDAATKGNPGRSACAIIIKENSQRYTFTHDLGEMDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSmMQG 80
Cdd:COG0328    2 MIEIYTDGACRGNPGPGGWGAVIRYGGEEKELSGGLGDTTNNRAELTALIAALEALKELGPCEVEIYTDSQYVVNQ-ITG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488370374  81 KVKNAKFKVYFE--NIEILEQSFDLM-----FVRWIPRKQ----NKEANQLAQQTL 125
Cdd:COG0328   81 WIHGWKKNGWKPvkNPDLWQRLDELLarhkvTFEWVKGHAghpgNERADALANKAL 136
rnhA PRK13907
ribonuclease H; Provisional
 1-125 1.07e-25

ribonuclease H; Provisional


Pssm-ID: 139967 [Multi-domain]  Cd Length: 128  Bit Score: 93.58  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374   1 MAKIHFDAATKGNPGRSACAIIIKENSQRYTFTHDLGEMDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSMMQG 80
Cdd:PRK13907   1 MIEVYIDGASKGNPGPSGAGVFIKGVQPAVQLSLPLGTMSNHEAEYHALLAALKYCTEHNYNIVSFRTDSQLVERAVEKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488370374  81 KVKNAKFKVYFENIEILEQSFDLMFVRWIPRKQNKEANQLAQQTL 125
Cdd:PRK13907  81 YAKNKMFAPLLEEALQYIKSFDLFFIKWIPSSQNKVADELARKAI 125
RVT_3 pfam13456
Reverse transcriptase-like; This domain is found in plants and appears to be part of a ...
 6-122 2.13e-14

Reverse transcriptase-like; This domain is found in plants and appears to be part of a retrotransposon.


Pssm-ID: 433223 [Multi-domain]  Cd Length: 123  Bit Score: 64.59  E-value: 2.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374    6 FDAATKGNPGRSACAIIIK-ENSQRYTFTHD--LGEMDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSMMQGKV 82
Cdd:pfam13456   2 FDGAFKCDSGLAGAGVVIRdPNGNVLLAGQKklGPGASVLEAEAQALIIGLQLAWKLGIRHLIVEGDSATVVQLINGRSP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 488370374   83 KNAKFKVYFENIEILEQSFDLMFVRWIPRKQNKEANQLAQ 122
Cdd:pfam13456  82 KQSKLANLLDEIRKLLKRFESVSFEHIPREQNRVADTLAK 121
 
Name Accession Description Interval E-value
RNase_HI_like cd09279
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ...
 3-125 1.19e-41

RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Most archaeal genomes contain only type 2 RNase H (RNase HII); however, a few contain RNase HI as well. Although archaeal RNase HI sequences conserve the DEDD active-site motif, they lack other common features important for catalytic function, such as the basic protrusion region. Archaeal RNase HI homologs are more closely related to retroviral RNase HI than bacterial and eukaryotic type I RNase H in enzymatic properties.


Pssm-ID: 260011 [Multi-domain]  Cd Length: 128  Bit Score: 134.14  E-value: 1.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374   3 KIHFDAATKGNPGRSACAIIIK-ENSQRYTFTHDLGE-MDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSMM-Q 79
Cdd:cd09279    2 TLYFDGASRGNPGPAGAGVVIYsPGGEVLELSERLGFpATNNEAEYEALIAGLELALELGAEKLEIYGDSQLVVNQLNgE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488370374  80 GKVKNAKFKVYFENIEILEQSFDLMFVRWIPRKQNKEANQLAQQTL 125
Cdd:cd09279   82 YKVKNERLKPLLEKVLELLAKFELVELKWIPREQNKEADALANQAL 127
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
1-125 5.43e-29

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 102.23  E-value: 5.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374   1 MAKIHFDAATKGNPGRSACAIIIKENSQRYTFTHDLGEMDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSmMQG 80
Cdd:COG0328    2 MIEIYTDGACRGNPGPGGWGAVIRYGGEEKELSGGLGDTTNNRAELTALIAALEALKELGPCEVEIYTDSQYVVNQ-ITG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488370374  81 KVKNAKFKVYFE--NIEILEQSFDLM-----FVRWIPRKQ----NKEANQLAQQTL 125
Cdd:COG0328   81 WIHGWKKNGWKPvkNPDLWQRLDELLarhkvTFEWVKGHAghpgNERADALANKAL 136
rnhA PRK13907
ribonuclease H; Provisional
 1-125 1.07e-25

ribonuclease H; Provisional


Pssm-ID: 139967 [Multi-domain]  Cd Length: 128  Bit Score: 93.58  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374   1 MAKIHFDAATKGNPGRSACAIIIKENSQRYTFTHDLGEMDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSMMQG 80
Cdd:PRK13907   1 MIEVYIDGASKGNPGPSGAGVFIKGVQPAVQLSLPLGTMSNHEAEYHALLAALKYCTEHNYNIVSFRTDSQLVERAVEKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488370374  81 KVKNAKFKVYFENIEILEQSFDLMFVRWIPRKQNKEANQLAQQTL 125
Cdd:PRK13907  81 YAKNKMFAPLLEEALQYIKSFDLFFIKWIPSSQNKVADELARKAI 125
RNase_H_like cd06222
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
 4-121 5.60e-19

Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions.


Pssm-ID: 259998 [Multi-domain]  Cd Length: 121  Bit Score: 76.20  E-value: 5.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374   4 IHFDAATKGNPGRSACAIIIKENSQRYT--FTHDLGEMDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSMMQGK 81
Cdd:cd06222    1 INVDGSCRGNPGPAGIGGVLRDHEGGWLggFALKIGAPTALEAELLALLLALELALDLGYLKVIIESDSKYVVDLINSGS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488370374  82 VKNAKFKVYFENIEILEQSFDLMFVRWIPRKQNKEANQLA 121
Cdd:cd06222   81 FKWSPNILLIEDILLLLSRFWSVKISHVPREGNQVADALA 120
RVT_3 pfam13456
Reverse transcriptase-like; This domain is found in plants and appears to be part of a ...
 6-122 2.13e-14

Reverse transcriptase-like; This domain is found in plants and appears to be part of a retrotransposon.


Pssm-ID: 433223 [Multi-domain]  Cd Length: 123  Bit Score: 64.59  E-value: 2.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374    6 FDAATKGNPGRSACAIIIK-ENSQRYTFTHD--LGEMDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSMMQGKV 82
Cdd:pfam13456   2 FDGAFKCDSGLAGAGVVIRdPNGNVLLAGQKklGPGASVLEAEAQALIIGLQLAWKLGIRHLIVEGDSATVVQLINGRSP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 488370374   83 KNAKFKVYFENIEILEQSFDLMFVRWIPRKQNKEANQLAQ 122
Cdd:pfam13456  82 KQSKLANLLDEIRKLLKRFESVSFEHIPREQNRVADTLAK 121
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 7-121 9.56e-08

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 49.21  E-value: 9.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374   7 DAATKGNPGRSAC---------AIIIKENSQRytfthdLGEMDNHSAEWAAMLHALEHARELKVSNALLFTDSKLIEDSM 77
Cdd:PRK07238   8 DGGSRGNPGPAGYgavvwdadrGEVLAERAEA------IGRATNNVAEYRGLIAGLEAAAELGATEVEVRMDSKLVVEQM 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488370374  78 mQG--KVKNAKFKVYFENIEILEQSFDLMFVRWIPRKQNKEANQLA 121
Cdd:PRK07238  82 -SGrwKVKHPDMKPLAAQARELASQFGRVTYTWIPRARNAHADRLA 126
PRK07708 PRK07708
hypothetical protein; Validated
 4-125 3.33e-06

hypothetical protein; Validated


Pssm-ID: 181088 [Multi-domain]  Cd Length: 219  Bit Score: 44.25  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374   4 IHFDAATKGNPGRSACAIII--KENSQRYTFTHD--LGEM-DNHSAEWAAMLHALEHARELKVS-NALLFTDSKLIEDSM 77
Cdd:PRK07708  76 VYFDGGFDKETKLAGLGIVIyyKQGNKRYRIRRNayIEGIyDNNEAEYAALYYAMQELEELGVKhEPVTFRGDSQVVLNQ 155

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488370374  78 MQGK--VKNAKFKVYFENIEILEQSFDLMFV-RWIPRKQNKEANQLAQQTL 125
Cdd:PRK07708 156 LAGEwpCYDEHLNHWLDRIEQKLKQLKLTPVyEPISRKQNKEADQLATQAL 206
RNase_H_Dikarya_like cd13934
Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many ...
 16-123 2.02e-03

Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many of which are uncharacterized. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication.


Pssm-ID: 260014 [Multi-domain]  Cd Length: 153  Bit Score: 36.02  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374  16 RSACAIIIKENSqRYTFTHDLGEMDNHS-----AEWAAMLHALEHAREL------KVSNALLFTDSKLIEDSM---MQGK 81
Cdd:cd13934   17 RAGYGVYFGPDS-SYNVSGRLEDTGGHPqtsqrAELRAAIAALRFRSWIidpdgeGLKTVVIATDSEYVVKGAtewIPKW 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488370374  82 V----KNAKFK--VYFENIEILEQSFDLMF-----VRW--IPRKQNKEANQLAQQ 123
Cdd:cd13934   96 KrngwRTSKGKpvKNRDLFELLLDEIEDLEeggveVQFwhVPRELNKEADRLAKA 150
RNase_HI_eukaryote_like cd09280
Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic ...
 44-123 8.83e-03

Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic counterparts; Ribonuclease H (RNase H) is classified into two families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. Eukaryotic RNase H is longer and more complex than in prokaryotes. Almost all eukaryotic RNase HI have highly conserved regions at their N-termini called hybrid binding domain (HBD). It is speculated that the HBD contributes to binding the RNA/DNA hybrid. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability, but RNase H is essential in higher eukaryotes. RNase H knockout mice lack mitochondrial DNA replication and die as embryos.


Pssm-ID: 260012 [Multi-domain]  Cd Length: 145  Bit Score: 34.08  E-value: 8.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370374  44 AEWAAMLHALEHARELKVSNALLFTDSK-LIE------DSMMQGKVKNAKFKvYFENIEILEQSFDLMFVRWIPRK---- 112
Cdd:cd09280   46 AELLAVIHALEQAPEEGIRKLEIRTDSKyAINcitkwiPKWKKNGWKTSKGK-PVKNQDLIKELDKLLRKRGIKVKfehv 124

                         90
                 ....*....|....*...
gi 488370374 113 -------QNKEANQLAQQ 123
Cdd:cd09280  125 kghsgdpGNEEADRLARE 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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